NIKQ_RHOCB
ID NIKQ_RHOCB Reviewed; 284 AA.
AC D5AQY7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Nickel transport protein NikQ;
DE AltName: Full=Energy-coupling factor transporter transmembrane protein NikQ;
DE Short=ECF transporter T component NikQ;
GN Name=nikQ; Synonyms=cbiQ1; OrderedLocusNames=RCAP_rcc01033;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [2]
RP FUNCTION IN NICKEL TRANSPORT, SUBSTRATES, SUBUNIT, AND EXPRESSION IN
RP E.COLI.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=16352848; DOI=10.1128/jb.188.1.317-327.2006;
RA Rodionov D.A., Hebbeln P., Gelfand M.S., Eitinger T.;
RT "Comparative and functional genomic analysis of prokaryotic nickel and
RT cobalt uptake transporters: evidence for a novel group of ATP-binding
RT cassette transporters.";
RL J. Bacteriol. 188:317-327(2006).
CC -!- FUNCTION: Part of the energy-coupling factor (ECF) transporter complex
CC NikMNQO involved in nickel import. The complex confers nickel uptake
CC upon expression in E.coli; can also transport cobalt with a very low
CC affinity. {ECO:0000269|PubMed:16352848}.
CC -!- SUBUNIT: Forms an energy-coupling factor (ECF) transporter complex
CC composed of an ATP-binding protein (A component, NikO), a transmembrane
CC protein (T component, NikQ) and a fused possible substrate-capture
CC protein (S component, NikMN) of unknown stoichimetry. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbiQ family. {ECO:0000305}.
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DR EMBL; CP001312; ADE84793.1; -; Genomic_DNA.
DR AlphaFoldDB; D5AQY7; -.
DR SMR; D5AQY7; -.
DR STRING; 272942.RCAP_rcc01033; -.
DR TCDB; 3.A.1.23.7; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE84793; ADE84793; RCAP_rcc01033.
DR KEGG; rcp:RCAP_rcc01033; -.
DR eggNOG; COG0619; Bacteria.
DR HOGENOM; CLU_056469_1_0_5; -.
DR OMA; MCYRYIF; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro.
DR GO; GO:0015675; P:nickel cation transport; IDA:UniProtKB.
DR InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane.
DR InterPro; IPR012809; ECF_CbiQ.
DR Pfam; PF02361; CbiQ; 1.
DR TIGRFAMs; TIGR02454; ECF_T_CbiQ; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Nickel;
KW Nickel transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..284
FT /note="Nickel transport protein NikQ"
FT /id="PRO_0000411085"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 284 AA; 29859 MW; 8AB110F4A2053548 CRC64;
MTDPSVVHAR APAPDRIGRL GAGVRGLMQH AEEAAGLAQR PGLLQGLDPR AKVAGAFALI
LAAVATRSLL VLLALFVLAT ALAAASQISP ARLARQVWIV VLGFTGMIAL PALILVPGTP
VLSLPFGLAI TEQGLRAAAF LTGRSETTAT LALALVLTTP WPQVLKALRC LGVPRAAVMI
LGMTHRYIFV LADLALDLFE ARRSRLVGRL SPAEARRLAT GIAGALFERA LALSSEVHLA
MLARGWRGEV HLIDDFRFRP RDGGALVLAA AILAGVVWAG SVWP